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Award Information
Agency: Department of Health and Human Services
Branch: N/A
Contract: GM54958-01
Agency Tracking Number: 39159
Amount: $92,648.00
Phase: Phase I
Program: SBIR
Solicitation Topic Code: N/A
Solicitation Number: N/A
Solicitation Year: N/A
Award Year: 1997
Award Start Date (Proposal Award Date): N/A
Award End Date (Contract End Date): N/A
Small Business Information
12345 W 52ND AVE
Wheat Ridge, CO 80033
United States
HUBZone Owned: No
Woman Owned: No
Socially and Economically Disadvantaged: No
Principal Investigator
 () -
Business Contact
Phone: (303) 940-2312
Research Institution

Amino acid are the main components of proteins and are important elementary nutrients for living organisms. They are also valuable synthetic intermediates for the preparation of a large array of biologically active compounds important to the pharmaceutical industry. Examples of drugs based on amino acids are L-DOPA, L-tryptophan, and beta-lactam antibiotics. Unfortunately, typical production methods for amino acids require expensive and time-consuming optical resolutions to obtain optically pure products. A more desirable way to prepare amino acids would be to enantioselectively hydrogenate carbon-nitrogen double bond (C=N) groups of amino acid precursors. This direct synthesis route could lower costs because only the desired product is formed avoiding the expense of a chiral separation. Unfortunately, the current catalysts generally are not sufficiently active or selective enough to be industrially useful. The objective of this proposal is to prepare optically pure amino acids by enantioselective hydrogenation of compounds with C=N bonds and to show that a variety of amino acids can be economically produced on an industrial scale. PROPOSED COMMMERCIAL APPLICATION This research will lead to the development general method for the production of optically pure amino acids by the enantioselective hydrogenation of compounds with C=N bonds. This will allow the economical production of valuable amino acids for use as pharmaceuticals and synthetic intermediates. $ = TOTAL AWARD AMTS & NOT LIMITED TO PORTION OF PROJECT RELATED TO SUBJECT OF SEARCH SUBPROJECT $ = TOTAL AWARD AMOUNT DIVIDED BY NUMBER OF SUBPROJECTS SOURCE: CRISP FORMAT F FY 97 LAST UPDATE 04-07-98 1QUERY 1536 ID SEARCH 06/01/98 PAGE 326 --PROJECT NUMBER......1 R43 GM54976-01A1 INVESTIGATOR NAME/ADDRESS FY 97 SHUMAN, BARRY M IRG/INTRAMURAL UNIT..ZRG2 BIOSOURCE INTERNATIONAL INC AWARD AMOUNT......... $99,905 820 FLYNN ROAD CAMARILLO CA 93012 PERFORMING ORGANIZATION: BIOSOURCE INTERNATIONAL, INC. TITLE LUCIFERASE SYSTEM FOR NUCLEIC ACID DETECTION ABSTRACT: DESCRIPTION: (Adapted from the Applicant's Abstract). The goal is to develop a luminescent bacterial luciferase system for the nonradioactive detection of nucleic acids. Bacterial luciferase from Vibrio harveyi is an enzyme that catalyzes the reaction of reduced flavin mononucleotide (FMNH2), molecular oxygen, and a long-chain aliphatic aldehyde to yield the oxidize flavin mononucleotide (FMN), the corresponding long-chain carboxylic acid, and light. The investigators have designed an analogue of FMN that consists of a 2'- deoxyuridine molecule covalently bound to a flavin mononucleotide through a polymethylene linker arm. This analogue has the following desirable properties: 1) it can be easily prepared using existing methodologies; 2) it can be conveniently linked to a oligonucleotide; and most importantly 3) the analogue (in its reduced form) should be an effective substrate for luciferase. This technology has applications in DNA sequencing and nucleic acid hybridization procedures. This flavin-luciferase system is expected to be comparable to existing non radioactive DNA detection methods in sensitivity, yet superior in terms of the resolution obtained. In this method the luminescent species is fixed to the oligonucleotide, while in other methods the luminescent species is released from the oligonucleotide at a high turnover number. This rapid turnover of luminescent molecules compromises the resolution obtained. $ = TOTAL AWARD AMTS & NOT LIMITED TO PORTION OF PROJECT RELATED TO SUBJECT OF SEARCH SUBPROJECT $ = TOTAL AWARD AMOUNT DIVIDED BY NUMBER OF SUBPROJECTS SOURCE: CRISP FORMAT F FY 97 LAST UPDATE 04-07-98 1QUERY 1536 ID SEARCH 06/01/98 PAGE 327 --PROJECT NUMBER......2 R44 GM54991-02A1 INVESTIGATOR NAME/ADDRESS FY 97 SHLYAKHTENKO, LUDA S IRG/INTRAMURAL UNIT..ZRG2 ARIZONA STATE UNIVERSITY AWARD AMOUNT......... $245,296 BOX 87270 TEMPE, AZ 85287-2701 PERFORMING ORGANIZATION: BIOFORCE LABORATORY TITLE FUNCTIONAL SUBSTRATES FOR SCANNING PROBE MICROSCOPY ABSTRACT: Progress towards rapid and simple characterization of biomolecular samples by scanning probe microscopy (SPM) is impeded considerably by limitations of the current approach to sample preparation. The group at Arizona State University, with which BioForce Laboratory has started a collaboration, pioneered a simple and versatile approach based on chemical functionalization of mica. Keeping in mind the positive results obtained under Phase I with AP-mica, methylated mica and in particular chemically reactive iodopropyl mica, we propose in Phase II to develop further chemical modification procedures of surfaces with silanes. The ultimate goal of these studies is to obtain surfaces with almost any desirable characteristics. These include negatively and positively charged surfaces having different controlled charge densities and surfaces with a selective binding affinity towards specific groups of macromolecules. The last feature is extremely important for making easier the use of AFM as the instrument for studies of intermolecular interactions, a very attractive application of AFM for future pharmaceutical studies and in particular for drug design. In this connection, a significant part of our efforts will also be devoted to the development of technologies for preparation of functionalized tips. Functionalized substrates may also be useful in optical and near-field scanning optical microscopy and for preparation of biomolecular chips.

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